Rennin

Rennin, also known as Chymosin, is a pepsin-related proteolytic enzyme synthesized by cells in the stomach of certain animals that efficiently converts liquid milk into a semi-solid, allowing it to remain in the stomach for longer. The natural substrate of Rennin is K-casein, which is specifically cleaved at the peptide bond between amino acid residues 105 and 106, phenylalanine and methionine, and is widely used in cheese production^[1].

This product is derived fro M plant separation and can be used for emulsion coagulation. The amount of chymosin added is directly proportional to the coagulation time. The more added, the faster the coagulation time.

Molecular weight: 36 KDa
Temperature range: effective temperature range 35-95 ℃, optimal temperature 35-37 ℃;
pH range: effective p h range 5-8, optimal ph value 6.1-6.2;
Inhibitors: Fe³⁺, Cu²⁺, Hg⁺, Pb⁺
Solvent: water

References:
[1]. Gilliland GL, et al. Dill J. Functional implications of the three-dimensional structure of bovine chymosin. Adv Exp Med Biol. 1991;306:23-37.

Rennin，也称 Chymosin，是一种与胃蛋白酶相关的蛋白水解酶，由某些动物胃中的细胞合成，可有效地将液态奶转化为半固体，使其在胃中停留更长时间。Rennin 的天然底物是 K-酪蛋白，它在氨基酸残基 105 和 106、苯丙氨酸和甲硫氨酸之间的肽键处被特异性切割，可广泛用于奶酪的生产。

本产品来源于植物分离，可用于乳液凝结，凝乳酶添加量与凝乳时间成正比，添加量越多，凝乳时间越快。

分子量：36 KDa
温度范围：有效温度范围35-95℃，最适温度 35-37℃；
pH 范围： 有效 pH 范围 5-8，最适 pH 值 6.1-6.2；
抑制剂：Fe³⁺、Cu²⁺、Hg⁺、Pb⁺
溶剂：水